HFI1_SCHPO
ID HFI1_SCHPO Reviewed; 339 AA.
AC O94301;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Transcriptional coactivator hfi1;
GN Name=hfi1; ORFNames=SPBC887.18c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation. At
CC the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction and promoter selectivity, interaction with transcription
CC activators, and chromatin modification through histone acetylation and
CC deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent
CC (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA
CC via upstream activating sequences (UASs). SALSA, an altered form of
CC SAGA, may be involved in positive transcriptional regulation. SLIK is
CC proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the SAGA, SALSA and SLIK complexes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the HFI1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21903.1; -; Genomic_DNA.
DR PIR; T40743; T40743.
DR RefSeq; NP_596492.1; NM_001022412.2.
DR AlphaFoldDB; O94301; -.
DR SMR; O94301; -.
DR BioGRID; 277716; 20.
DR IntAct; O94301; 20.
DR MINT; O94301; -.
DR STRING; 4896.SPBC887.18c.1; -.
DR MaxQB; O94301; -.
DR PaxDb; O94301; -.
DR EnsemblFungi; SPBC887.18c.1; SPBC887.18c.1:pep; SPBC887.18c.
DR GeneID; 2541202; -.
DR KEGG; spo:SPBC887.18c; -.
DR PomBase; SPBC887.18c; hfi1.
DR VEuPathDB; FungiDB:SPBC887.18c; -.
DR eggNOG; ENOG502RX84; Eukaryota.
DR HOGENOM; CLU_802061_0_0_1; -.
DR InParanoid; O94301; -.
DR OMA; MLVEEYP; -.
DR PhylomeDB; O94301; -.
DR PRO; PR:O94301; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR InterPro; IPR024738; Hfi1/Tada1.
DR PANTHER; PTHR21277; PTHR21277; 1.
DR Pfam; PF12767; SAGA-Tad1; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..339
FT /note="Transcriptional coactivator hfi1"
FT /id="PRO_0000372427"
SQ SEQUENCE 339 AA; 37946 MW; 24BAB9EE42F55A2A CRC64;
MTEGVTVQKV QSASSNGHKP NTVISQIISE MQSLLGSSFE VYTKTMTDFL IGQLSRKEMK
SMLLTFAGKS NFDKLHNSII FHILKLMQKN NDTFSALHHL PWFKRKKVDN SLFLHKKISS
QNAQVRLIKR IVMSLSYKDR ARIKTALKEK PVTPSLISGL LLETRIAKLP KIPVSRDKLN
SVFVNDIKAG YVAPLACETL ELPDSESLKE RITAISLENG LLGGVQKGVS DIILAGLESH
LKNILSRCFS ILNKNIRQKN TENDAAGFTI NDLNLAWTIE PHAFVEQYPQ KLRMPFLLHD
SYTEDEISIC AESPSYMLAS NDAQSDRNSV ASLLDEVLS
